SDR: Structure, mechanism of action, and substrate recognition

被引：90

作者：

Tanaka, N

Nonaka, T

Nakamura, KT

Hara, A

机构：

[1] Showa Univ, Sch Pharmaceut Sci, Shinagawa Ku, Tokyo 1428555, Japan

[2] Nagaoka Univ Technol, Dept Bioengn, Nagaoka, Niigata 9402188, Japan

[3] Gifu Pharmaceut Univ, Biochem Lab, Gifu 5028585, Japan

来源：

CURRENT ORGANIC CHEMISTRY | 2001年 / 5卷 / 01期

关键词：

D O I：

10.2174/1385272013375751

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

Short-chain dehydrogenases/reductases (SDR) constitute a large protein family. The SDR family now includes more than 1,000 enzymes from humans, mammals, insects and bacteria, and exhibits a wide variety of substrate specificity for steroids, retinoids, prostaglandins, sugars, alcohols and other small molecules. These enzymes have a residue identity level of 15-30 %. Much has been done in the last decade to understand the structure-function relationships in the SDR enzymes. This review summarizes recent progress of structural and functional studies of the enzymes belonging to the SDR family (X-ray crystal structure analyses and site-directed mutagenesis studies). Based on these studies, the three-dimensional structure, catalytic mechanism, coenzyme specificity, and substrate specificity of the SDR enzymes are discussed.

引用

收藏

页码：89 / 111

页数：23

相关论文

共 83 条

[31] Isoleucine-15 of rainbow trout carbonyl reductase-like 20β-hydroxysteroid dehydrogenase is critical for coenzyme (NADPH) binding [J].

Guan, GJ ;

Todo, T ;

Tanaka, M ;

Young, G ;

Nagahama, Y .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (07) :3079-3083

[32] Dehydroepiandrosterone and dihydrotestosterone recognition by human estrogenic 17β-hydroxysteroid dehydrogenase -: C-18/C-19 steroid discrimination and enzyme-induced strain [J].

Han, Q ;

Campbell, RL ;

Gangloff, A ;

Huang, YW ;

Lin, SX .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (02) :1105-1111

[33] Function of human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase in androgen metabolism [J].

He, XY ;

Merz, G ;

Yang, YZ ;

Pullakart, R ;

Mehta, P ;

Schulz, H ;

Yang, SY .

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, 2000, 1484 (2-3) :267-277

[34]

Hülsmeyer M, 1998, PROTEIN SCI, V7, P1286

[35] CLONING AND SEQUENCING OF THE GENE ENCODING THE 72-KILODALTON DEHYDROGENASE SUBUNIT OF ALCOHOL-DEHYDROGENASE FROM ACETOBACTER-ACETI [J].

INOUE, T ;

SUNAGAWA, M ;

MORI, A ;

IMAI, C ;

FUKUDA, M ;

TAKAGI, M ;

YANO, K .

JOURNAL OF BACTERIOLOGY, 1989, 171 (06) :3115-3122

[36]

IUPAC, 1983, EUR J BIOCHEM, V131, P9, DOI DOI 10.1021/IC2011716

[37] SHORT-CHAIN DEHYDROGENASES REDUCTASES (SDR) [J].

JORNVALL, H ;

PERSSON, B ;

KROOK, M ;

ATRIAN, S ;

GONZALEZDUARTE, R ;

JEFFERY, J ;

GHOSH, D .

BIOCHEMISTRY, 1995, 34 (18) :6003-6013

[38] ALCOHOL AND POLYOL DEHYDROGENASES ARE BOTH DIVIDED INTO 2 PROTEIN TYPES, AND STRUCTURAL-PROPERTIES CROSS-RELATE THE DIFFERENT ENZYME-ACTIVITIES WITHIN EACH TYPE [J].

JORNVALL, H ;

PERSSON, M ;

JEFFERY, J .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1981, 78 (07) :4226-4230

[39] SDR and MDR:: completed genome sequences show these protein families to be large, of old origin, and of complex nature [J].

Jörnvall, H ;

Höög, JO ;

Persson, B .

FEBS LETTERS, 1999, 445 (2-3) :261-264

[40]

Kiefer PM, 1996, J BIOL CHEM, V271, P3437

← 1 2 3 4 5 6 7 8 9 →